Information on EC 3.6.5.1 - heterotrimeric G-protein GTPase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
3.6.5.1
-
RECOMMENDED NAME
GeneOntology No.
heterotrimeric G-protein GTPase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GTP + H2O = GDP + phosphate
show the reaction diagram
-
-
-
-
GTP + H2O = GDP + phosphate
show the reaction diagram
binding and hydrolysis of GTP triggers reciprocal conformational changes within a switch region within the catalytic domain
-
GTP + H2O = GDP + phosphate
show the reaction diagram
mechanism of membrane translocation
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis
Saccharomyces pombe
-
-
hydrolysis
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
phosphorous acid anhydride hydrolysis
-
-
-
-
phosphorous acid anhydride hydrolysis
-
-
phosphorous acid anhydride hydrolysis
-
-
phosphorous acid anhydride hydrolysis
-
-
phosphorous acid anhydride hydrolysis
-
-
phosphorous acid anhydride hydrolysis
-
-
phosphorous acid anhydride hydrolysis
-
-
PATHWAY
KEGG Link
MetaCyc Link
NIL
-
SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (signalling)
This group comprises GTP-hydrolysing systems, where GTP and GDP alternate in binding. This group includes stimulatory and inhibitory G-proteins such as Gs, Gi, Go and Golf, targetting adenylate cyclase and/or K+ and Ca2+ channels; Gq stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase. Golf is instrumental in odour perception, transducin in vision and gustducin in taste recognition. At least 16 different alpha subunits (39-52 kDa), 5 beta subunits (36 kDa) and 12 gamma subunits (6-9 kDa) are known.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cone transducin
-
-
EC 3.6.1.46
-
-
formerly
-
elongation factor 2
-
-
G alpha i2
-
-
G alpha q
-
-
G alpha11
-
-
G alphaQ
-
-
G betagamma
-
-
Galpha-subunit
Saccharomyces pombe
-
-
GPA1
Saccharomyces pombe
-
-
Gs alpha
-
-
GTP phosphohydrolase
-
-
-
-
GTP phosphohydrolase
-
-
GTP phosphohydrolase
-
-
GTP phosphohydrolase
-
-
GTP phosphohydrolase
-
-
GTP phosphohydrolase
-
-
GTP phosphohydrolase
-
-
GTPase
-
-
-
-
guanosine 5'-triphosphatase
-
-
-
-
guanosine triphosphatase
-
-
-
-
heterotrimeric G protein
-
-
heterotrimeric G protein
-
-
heterotrimeric G protein
Saccharomyces pombe
-
-
heterotrimeric G protein alpha subunit
-
-
heterotrimeric G protein family
-
-
heterotrimeric G protein Gsalpha
P63091
-
heterotrimeric G-protein
-
-
heterotrimeric G-protein
-
-
heterotrimeric G-protein GTPase
-
-
heterotrimeric G-protein GTPase
-
-
heterotrimeric G-protein GTPase
-
-
heterotrimeric G-protein GTPase
-
-
heterotrimeric G-protein GTPase
-
-
heterotrimeric G-protein GTPase
-
-
heterotrimeric G-protein GTPase
-
-
heterotrimeric G-protein GTPase
-
-
heterotrimeric GTPase
-
-
heterotrimeric GTPase
-
-
phosphatase, guanosine tri-
-
-
-
-
photoreceptor-specific G protein
-
-
Rab1
-
-
Rab1 GTPase
-
-
Rab1a
-
there are two isoforms, Rab1a and Rab1b
ribosomal GTPase
-
-
-
-
transducin
-
-
transducin
-
-
transducin GTPase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9059-32-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
a mixture of trimeric Gq and G11, referred to as Gq/11
-
-
Manually annotated by BRENDA team
alpha-subunit of transducin
-
-
Manually annotated by BRENDA team
Go and Gs
-
-
Manually annotated by BRENDA team
Go: a G protein with unknown function
-
-
Manually annotated by BRENDA team
Goalpha
-
-
Manually annotated by BRENDA team
photoreceptor G protein transducin
-
-
Manually annotated by BRENDA team
taste-specific G protein, gustducin
-
-
Manually annotated by BRENDA team
Aspergillus Emericella nidulans
-
-
Manually annotated by BRENDA team
cv. Jack Seeds
-
-
Manually annotated by BRENDA team
cv. Jack Seeds, four soybean Galpha proteins GmGalpha1-4
-
-
Manually annotated by BRENDA team
transducin GTPase activity
-
-
Manually annotated by BRENDA team
recombiant protein expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
alpha subunit of transducin
-
-
Manually annotated by BRENDA team
alpha subunit of transducin
-
-
Manually annotated by BRENDA team
Gi1alpha, Gi2alpha anf Gi3alpha
-
-
Manually annotated by BRENDA team
Gialpha1
-
-
Manually annotated by BRENDA team
Sprague-Dawley rat
-
-
Manually annotated by BRENDA team
Rattus norvegicus Gialpha1
Gialpha1
-
-
Manually annotated by BRENDA team
Saccharomyces pombe
-
-
-
Manually annotated by BRENDA team
recombinant protein expressed in baculovirus/Sf9 system, reconstituted in vesicles
-
-
Manually annotated by BRENDA team
Gi: the G protein that mediates inhibition of adenylate cyclase
-
-
Manually annotated by BRENDA team
GTPase that functions as a component of the rhodopsin-linked, light-activated phosphodiesterase system
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
phylogenetic comparison of genes involved in the heterotrimeric G-proteins signaling system, detailed overview over eukaryotic lineages and structural similarities. Identification of heterotrimeric G-protein subunits, RGS domain proteins and 7TM receptors. Through much of eukaryotic evolution, cells contain both 7TM receptors that acted as GEFs and those as GAPs (with C-terminal RGS domains) for Galphas
evolution
-
Galpha subunits are classified into four subfamilies, Gs, Gi, Gq and G12. Galpha12/13 and Galphaq are directly involved in the activation of RhoGTPases, molecular mechanisms for regulation of RhoGTPase activity through GPCR heterotrimeric G12/13-signalling pathways, overview. The G12/13-RH-RhoGEF signalling mechanism is well conserved over species
evolution
-
expression of four Galpha, four Gbeta, and two Ggamma proteins, expression profiles by quantitative PCR, the four Galpha proteins form two distinct groups based on their GTPase activity. The proteins interact in most of the possible combinations, with some degree of interaction specificity between duplicated gene pairs
malfunction
-
deletion of any component of the Galpha13-RhoGEF-RhoA-signalling pathway results in a similar phenotype consisting of embryonic lethality at the stage of gastrulation
malfunction
-
overexpression of constitutively active Galpha12 or 13 induces several cellular effects which suggest stimulation of Rho activity in cells, such as formation of actin stress fibres or neurite retraction in neuronal cells. NIH3T3 transforming activity of constitutively active mutant of Galpha12 can be prevented by blocking its palmitoylation
metabolism
-
complex regulation of the G-protein cycle in soybean and in other plants with expanded G-protein networks
physiological function
-
the virulence factor and highly potent mitogen Pasteurella multocida toxin, PMT, exhibits its toxic activity through activation of heterotrimeric GTPase-dependent pathways, by deamidating a glutamine residue in the alpha subunit of these GTPases via its C-terminal C3 domain, mechanism, overview. Galpha11 and Galphaq are substrates for PMT. C-PMT deamidates Galphaq at least tenfold more efficiently than the full-length PMT. Mutant PMT C1165S is not active on the GTPases, while the mutant C-terminal part of PMT C1159S deamidates Gai/q
physiological function
-
the G12/13-RH-RhoGEF signalling mechanism is involved in critical steps for cell physiology and disease conditions. alpha Subunits of G12 or G13 interact with members of the RH domain containing guanine nucleotide exchange factors for Rho (RH-RhoGEF) family of proteins to directly connect G protein-mediated signalling and RhoGTPase signalling, G12/13-mediated signalling is one mechanism to regulate RhoGTPase activity in response to extracellular stimuli
physiological function
-
the G12/13-RH-RhoGEF signalling mechanism is involved in critical steps for cell physiology and disease conditions, including embryonic development, oncogenesis and cancer metastasis. alpha Subunits of G12 or G13 interact with members of the RH domain containing guanine nucleotide exchange factors for Rho (RH-RhoGEF) family of proteins to directly connect G protein-mediated signalling and RhoGTPase signalling, G12/13-mediated signalling is one mechanism to regulate RhoGTPase activity in response to extracellular stimuli. Wild-type Galpha12 is the only Galpha subunit that acts as an oncogene in NIH3T3 cells
physiological function
-
Galpha proteins regulate G-protein signaling working with RGS proteins
metabolism
-
the Galpha proteins form an elaborate heterotrimeric G-protein network
additional information
-
Gbetagamma interacts with the N-terminal alpha helix of Galpha through one of the seven bladed propellers of the Gbeta subunit
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
ir
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
Saccharomyces pombe
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
ir
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
Gi1alpha, Gi2alpha and Gi3alpha are capable of preventing stimulation of adenylate cyclase by the alpha2A-adrenoceptor
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
activates phosphoinositide-specific phospholipase C in the presence of aluminium fluoride
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
conformational change induced by the exchange of GDP for GTP in transducin and gustducin, taste-specific G protein, gustducin
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
photoreceptor G protein
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
Gi: the G protein that mediates inhibition of adenylate cyclase
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
intrinsic GTPase activity of transducin controls inactivation of the effector enzyme, cGMP phosphodiesterase during turnoff of the visual signal
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
GTPase that functions as a component of the rhodopsin-linked, light-activated phosphodiesterase system
-
-
-
GTP + H2O
GDP + phosphate
show the reaction diagram
-
GTPase that functions as a component of the rhodopsin-linked, light-activated phosphodiesterase system
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
cycle of G protein activation and deactivation that transmits a signal from receptor to effector: when GDP is bound the alpha subunit associated with the betagamma subunit to form an inactive heterotrimer that binds to the receptor. Both alpha and betagamma subunits can bind to the receptor. When a chemical or physical signal stimulates the receptor, the receptor becomes activated and changes its conformation. The GDP-ligated alpha-subunit responds with a conformational change that decreases GDP affinity, so that GDP is released. Leaving GDP is replaced by GTP. Once ATP is bound, the alpha subunit assumes its activated conformation and dissociates both from the receptor and from betagamma. The activated state lasts until the GTP is hydrolyzed to GDP by the intrinsic GTPase activity of the alpha-subunit. Once GTP is cleaved to GDP, the alpha and betagamma subunits reassociate, become inactive, and return to the receptor. The free alpha and betagamma subunits each activate target effectors. Galphas and Galphaolf, stimulate adenylyl cyclase and regulate Ca2+ channels. Galphai-1, Galphai-2, Galphai-3, Galphao, Galphat-1, Galphat-2, Galphagust and Galphaz inhibit adenylyl cyclase, regulate K+ and Ca2+ channels, and activate cGMP phosphodiesterase. Galphaq, Galpha11, Galpha14, Galppha15 and Galpha16 activate phospholipase C. Galpha12 and Galpha13 regulate Na/K+ exchange. The betagamma subunit is a positive regulator of K+ channels, adenylyl cyclase, phospholipase Cbeta, phospholipase A2, phosphoinositide 3-kinase and beta-adrenergic receptor kinase
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
Gq/11 is the physiological regulator of phospholipase C-beta1
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
Galpha subunits can regulate intracellular effectors, such as adenylyl cyclase, phospholipase Cbeta, K+ and Ca+ channels, and cyclic GMP phosphodiesterase
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
assay at pH 7.5, 15 mM MgCl
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
assay at pH 7.8, 30C, 30 min
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
usage of fluorescence-labeled 4,4-difluoro-4-bora-3alpha,4alpha-diaza-s-indacene-GTP substrate for assays
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
Rattus norvegicus Gialpha1
-
-
-
?
additional information
?
-
-
membrane translocation of RGS8, a regulator of G-protein signaling, depends on interaction of RGS8 with enzyme
-
-
-
additional information
?
-
-
calcium-independent PKCtheta/delta is a potential downstream target of Galpha12
-
-
-
additional information
?
-
-
Galpha12 and Galpha13 couple with G-protein coupled receptors, GPCRs, for various ligands, e.g. angiotensin II, endothelin, thrombin, bombesin, thromboxane A2, sphingosine-1-phosphate, and lysophosphatidic acid. The coupling specificity between G12 and G13 is usually not strict and most of these ligands can activate both G12 and G13. The RH domain of PDZ-RhoGEF interacts with Galpha13 through multiple intermolecular interfaces. One point of contact is centred on an Ile-Ile-Gly motif found N-terminal to the RGS box. This motif forms multiple contacts with the alpha helical domain of Galpha13, and is conserved in other RH-RhoGEFs. Additionally, Galpha13 interacts with an acidic stretch of residues N-terminal to the core RGS box of PDZ-RhoGEF, overview
-
-
-
additional information
?
-
-
protein-protein interaction analysis between soybean G-protein subunits, overview. GmGalpha and GmGbeta interact in most of the possible combinations
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
ir
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
ir
GTP + H2O
GDP + phosphate
show the reaction diagram
-
Gi1alpha, Gi2alpha and Gi3alpha are capable of preventing stimulation of adenylate cyclase by the alpha2A-adrenoceptor
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
taste-specific G protein, gustducin
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
photoreceptor G protein
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
Gi: the G protein that mediates inhibition of adenylate cyclase
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
intrinsic GTPase activity of transducin controls inactivation of the effector enzyme, cGMP phosphodiesterase during turnoff of the visual signal
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
GTPase that functions as a component of the rhodopsin-linked, light-activated phosphodiesterase system
-
-
-
GTP + H2O
GDP + phosphate
show the reaction diagram
-
cycle of G protein activation and deactivation that transmits a signal from receptor to effector: when GDP is bound the alpha subunit associated with the betagamma subunit to form an inactive heterotrimer that binds to the receptor. Both alpha and betagamma subunits can bind to the receptor. When a chemical or physical signal stimulates the receptor, the receptor becomes activated and changes its conformation. The GDP-ligated alpha-subunit responds with a conformational change that decreases GDP affinity, so that GDP is released. Leaving GDP is replaced by GTP. Once ATP is bound, the alpha subunit assumes its activated conformation and dissociates both from the receptor and from betagamma. The activated state lasts until the GTP is hydrolyzed to GDP by the intrinsic GTPase activity of the alpha-subunit. Once GTP is cleaved to GDP, the alpha and betagamma subunits reassociate, become inactive, and return to the receptor. The free alpha and betagamma subunits each activate target effectors. Galphas and Galphaolf, stimulate adenylyl cyclase and regulate Ca2+ channels. Galphai-1, Galphai-2, Galphai-3, Galphao, Galphat-1, Galphat-2, Galphagust and Galphaz inhibit adenylyl cyclase, regulate K+ and Ca2+ channels, and activate cGMP phosphodiesterase. Galphaq, Galpha11, Galpha14, Galppha15 and Galpha16 activate phospholipase C. Galpha12 and Galpha13 regulate Na/K+ exchange. The betagamma subunit is a positive regulator of K+ channels, adenylyl cyclase, phospholipase Cbeta, phospholipase A2, phosphoinositide 3-kinase and beta-adrenergic receptor kinase
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
Gq/11 is the physiological regulator of phospholipase C-beta1
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
Galpha subunits can regulate intracellular effectors, such as adenylyl cyclase, phospholipase Cbeta, K+ and Ca+ channels, and cyclic GMP phosphodiesterase
-
?
additional information
?
-
-
calcium-independent PKCtheta/delta is a potential downstream target of Galpha12
-
-
-
additional information
?
-
-
Galpha12 and Galpha13 couple with G-protein coupled receptors, GPCRs, for various ligands, e.g. angiotensin II, endothelin, thrombin, bombesin, thromboxane A2, sphingosine-1-phosphate, and lysophosphatidic acid. The coupling specificity between G12 and G13 is usually not strict and most of these ligands can activate both G12 and G13. The RH domain of PDZ-RhoGEF interacts with Galpha13 through multiple intermolecular interfaces. One point of contact is centred on an Ile-Ile-Gly motif found N-terminal to the RGS box. This motif forms multiple contacts with the alpha helical domain of Galpha13, and is conserved in other RH-RhoGEFs. Additionally, Galpha13 interacts with an acidic stretch of residues N-terminal to the core RGS box of PDZ-RhoGEF, overview
-
-
-
additional information
?
-
-
protein-protein interaction analysis between soybean G-protein subunits, overview. GmGalpha and GmGbeta interact in most of the possible combinations
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
-
Mg2+
-
required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
betagamma subunit of the hetreotrimeric G protein
-
the beta and gamma subunit of G protein form tightly associated complexes, large number of possible combinations of unique beta and gamma subunits, inhibition of steady-state GTP hydrolysis catalyzed by Gsalpha, Goalpha and myristoylated rGialpha2
-
betagamma subunit of the hetreotrimeric G protein
-
inhibits by selectively binding to and stabilization of the GDP-bound state
-
GDP
-
competitive inhibition
Gpp(NH)p
-
competitive inhibition
-
Pasteurella multocida toxin
-
deamidates glutamine-205 of G alphaI2 to glutamic acid, inhibits intrinsic GTPase activity, causes persistent activation of the G protein
-
pertussis toxin
-
pertussis toxin-catalysed ADP-ribosylation prevents functional contacts between G-protein-coupled receptors and the Gi-like G-proteins
-
pertussis toxin
-
pertussis toxin-catalysed ADP-ribosylation prevents functional contacts between G-protein-coupled receptors and the Gi-like G-proteins
-
phosducin
-
inhibits betagamma function in vitro
-
regulator of G protein signaling protein
Saccharomyces pombe
-
Gpa1 signaling suppressed by low stimulation
-
YM-254890
-
-
Leu-Gly-Asn repeat-enriched protein
-
LGN protein, GDP dissociation inhibitor, GDI, binds to the alpha subunit of transducin in the GDP-bound state
-
additional information
-
GTPase rate is unaffected when transducin alpha-subunit binds to the inhibitory gamma-subunit of cGMP phosphodiesterase, altough this binding is fast and of high affinity
-
additional information
-
GTPase activity of transducin is blocked by ADP-ribosylation
-
additional information
-
tubulin binds to Gs alpha, Gi alpha1 and Gq alpha, destabilize microtubules
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
AGS3 protein
-
G-protein signaling modulator 1, GPSM1, Human Genome Organization nomenclature
-
amyloid beta-peptide fragment (1-42)
-
stimulates GTPase activity
-
amyloid beta-peptide fragment (25-35)
-
stimulates GTPase activity
-
Axin protein
-
member of RA or E subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
Axin2 protein
-
member of RA or E subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
betagamma-subunit of transducin
-
from bovine retinal transducin and from rabbit liver, enhances activity of Goalpha
-
Carbachol
-
0.1 mM, in presence of regulator of G-protein signaling proteins such as RGS4, Gbeta5 with RGS6, RGS7, RGS9 or RGS11, but not carbachol alone
cell-surface receptors
-
of the seven-transmembrane-helix class, activated by catalyzing the exchange of GDP for GTP in the guanine nucleotide-binding site of the alpha-subunit
-
CIVIAKLKANLM amide
-
peptide derived from glucagon-like peptide, residues 329-340, 0.001 mM, 186% of basal GTPase activity
CIVIAKLKANLMCKTDIKCRLAK amide
-
peptide derived from glucagon-like peptide, residues 329-351, 0.001 mM, 595% of basal GTPase activity
CKTDIKCRLAK amide
-
peptide derived from glucagon-like peptide, residues 341-351, 0.001 mM, 216% of basal GTPase activity
D-AKAP2 protein
-
-
-
EGL-10 protein
-
egg-laying defective protein 10
-
FlbA protein
-
-
-
G component
-
can bind GTP and can support light-dependent and GTP-dependent phosphodiesterase activation
-
gamma-subunit of cGMP phosphodiesterase
-
accelerate GTP hydrolysis by transducin
-
gamma-subunit of cGMP phosphodiesterase
-
Arg33 and Arg36 in the polycationic region of the gamma-subunit of cGMP phosphodiesterase have a special function for the interaction with alpha-subunit of transducin
-
gamma-subunit of cGMP phosphodiesterase
-
accelerate GTP hydrolysis by transducin; the GTPase activating epitope is located within the C-terminal third of phosphodiesterase
-
GRK1 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
GRK2 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
GRK3 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
GRK4 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
GRK5 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
GRK6 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
GRK7 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
H component
-
MW 60000 Da, participates in the light-dependent activation of GTPase, G component requires the presence of H component for expression of GTPase activity
-
LARG protein
-
member of GEF or F subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
muscarinic acetylcholine receptors
-
receptor m1 activates, no activation by receptor m2
-
NDP kinase
-
can transfer the gamma-phosphate of ATP directly to GDP bound to the G protein, this phosphorylation results in the activation of the signal-coupling proteins
-
p115-RhoGEF protein
-
member of GEF or F subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
Pasteurella multocida toxin
-
-
-
Pasteurella multocida toxin
-
dependent on cycling of G betagamma-subunits
-
Pasteurella multocida toxin
-
-
-
PDZ-RhoGEF protein
-
member of GEF or F subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
phenylephrine
-
-
phospholipase C-beta1
-
activating protein for Gq/11, its physiologic regulator
-
phospholipase D
-
coincubation of enzyme with phospholipase D in equal amounts stimulates up to 35%
-
regulator of G protein signaling protein
Saccharomyces pombe
-
Gpa1 signaling potentiated by high stimulation
-
RGS
-
retinal specific member of the RGS family accelerates GTP hydrolysis by transducin
RGS
-
stimulates
RGS
-
regulator of G-protein signaling
RGS1 protein
-
human B-lymphocyte, member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS1 protein
-
G-protein signaling proteins, RGS proteins, accelerate the inherent GTPase activity of Galpha proteins. The GTPase-accelerating activities of GmRGS1 and -2 differ for each GmGalpha. Differential effects of GmRGS1 and GmRGS2 on GmGalpha1-4 result from a single valine versus alanine difference. GmRGS protein sequence comparisons and expression pattern, overview
-
RGS10 protein
-
member of R12 or D subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS11 protein
-
member of R7 or C subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS12 protein
-
member of R12 or D subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS13 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS14 protein
-
-
-
RGS14 protein
-
member of R12 or D subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS16 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS16 protein
-
-
-
RGS17 protein
-
member of RZ or A subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS18 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS19 protein
-
member of RZ or A subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS2 protein
-
human T-lymphocyte, member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS2 protein
-
G-protein signaling proteins, RGS proteins, accelerate the inherent GTPase activity of Galpha proteins. The GTPase-accelerating activities of GmRGS1 and -2 differ for each GmGalpha. Differential effects of GmRGS1 and GmRGS2 on GmGalpha1-4 result from a single valine versus alanine difference. GmRGS protein sequence comparisons and expression pattern, overview
-
RGS20 protein
-
member of RZ or A subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS21 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS22 protein
-
-
-
RGS3 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS4
-
-
-
RGS4 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS5 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS6 protein
-
member of R7 or C subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS7 protein
-
member of R7 or C subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS8 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS9
-
-
-
RGS9 protein
-
member of R7 or C subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS9-1 protein
-
short splice variant of RGS9, in complex with type 5 G protein beta-subunit Gbeta5L, regulated by the membrane anchor R9AP
-
RGS9d protein
-
-
-
rhodopsin
-
transducin is activated by photoexcited rhodopsin which catalyzes the exchange of transducin-bound GDP for GTP and then stays active until bound GTP is hydrolyzed by the intrinsic GTPase activity
rhodopsin
-
photolyzed but not dark rhodopsin stimulates
SNX13 protein
-
member of SNX or H subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
SNX14 protein
-
member of SNX or H subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
SNX25 protein
-
member of SNX or H subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
Sst2 protein
-
Sst2: supersensitivity to pheromone-2
-
tubulin
P63091
direct transfer of GTP
-
unidentified membrane factor
-
accelerate GTP hydrolysis by transducin
-
LGN protein
-
G-protein signaling modulator 2, GPSM2, Human Genome Organization nomenclature
-
additional information
-
stimulation by mouse regulator of G-protein signaling RGS18 by interaction with the alpha subunit of both Gi and Gq subfamilies, RGS18 accelerates intrinsic GTPase activity of Galphai
-
additional information
-
presence of regulator of G-protein signaling proteins such as RGS4, Gbeta5 with RGS6, RGS7, RGS9 or RGS11 stimulates GTPase activity, additional presence of 0.1 mM carbachol stimulates further
-
additional information
-
GTPase activity is stimulated by ribosomes
-
additional information
-
GTPase activity is stimulated by ribosomes up to 2000fold
-
additional information
-
tubulin binds to G beta1gamma1, promotes microtubule stability
-
additional information
-
tubulin binds to Gs alpha
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0008
-
GTP
-
A26GSsEF-2, 40% glycol
0.001
-
GTP
-
SsEF-2, 40% glycol
0.0036
-
GTP
-
illuminated uROS is used as source of photoexited rhodopsin required for transducin activation
0.0055
-
GTP
-
A26GSsEF-2, 10% glycol
0.0079
-
GTP
-
illuminated V8-uROS is used as source of photoexited rhodopsin required for transducin activation
0.0096
-
GTP
-
SsEF-2, 10% glycol
0.0194
-
GTP
-
A26GSsEF-2, 0% glycol
0.1
-
GTP
-
G36 protein, unmodified
0.85
-
GTP
-
G36 protein phosphorylated by protein kinase M-like kinase
additional information
-
additional information
-
kinetics of 2'-/3'-O-N'-methylanthraniloyl-labeled GTP/GDP exchange for GmGalpha1-GmGalpha4, overview. GmGalpha1 and GmGalpha4 bind GTP more rapidly thanGmGalpha2 and GmGalpha3
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0018
-
GTP
-
GtalphaQ200L
0.012
-
GTP
-
30C, pH 5, presence of CuCl2, 2 mM
0.019
-
GTP
-
Gtalpha
0.144
-
GTP
-
30C, pH 5, presence of NiCl2, 2 mM
0.186
-
GTP
-
30C, pH 5, presence of FeCl2, 2 mM
0.2
-
GTP
-
SsEF-2, 10% glycol
0.486
-
GTP
-
30C, pH 5, presence of MnCl2, 2 mM
0.6
-
GTP
-
30C, pH 6, presence of CaCl2, 2 mM
1.14
-
GTP
-
30C, pH 6, presence of MgCl2, 2 mM
1.554
-
GTP
-
30C, pH 4, presence of NaCl, 2 mM
1.74
-
GTP
-
30C, pH 4, presence of KCl, 2 mM
1.9
-
GTP
-
SsEF-2, 40% glycol
2.118
-
GTP
-
30C, pH 4, presence of NH4Cl, 2 mM
7.2
-
GTP
-
A26GSsEF-2, 10% glycol
8
-
GTP
-
A26GSsEF-2, 0% glycol
9.9
-
GTP
-
A26GSsEF-2, 40% glycol
21
-
GTP
-
alpha-subunit of transducin
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0003
-
GDP
-
SsEF-2, 40% glycol
0.0005
-
GDP
-
A26GSsEF-2, 40% glycol
0.0074
-
GDP
-
A26GSsEF-2, 0% glycol
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.722
-
-
recombinant GL2
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
in presence of NH4Cl, NaCl, KCl
5
-
-
in presence of CuCl2, FeCl2, MnCl2, NiCl2
6
-
-
in presence of CaCl2, MgCl2
7.5
-
-
activity assay
7.5
-
-
assay at
7.8
-
-
activity assay
8
-
-
single-turnover GTPase assay
8
-
-
assay at
additional information
-
-
optimum pH-value depends on kation present
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
25
-
assay at
60
-
-
activity assay
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
24
-
activity assay
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
Go-alpha subunit
Manually annotated by BRENDA team
-
the relative levels of the G-protein alpha subunits GS alpha-L, GS alpha-S, Gialpha-1, Gialpha-2 and Goalpha are unchanged in membranes prepared from Alzheimer-diseased frontal cortex or hippocampus to control brains. The activity of the G-protein associated high affinity GTPase is reduced in the frontal cortex by 25% and in the hippocampus by 27%
Manually annotated by BRENDA team
-
synaptic membrane
Manually annotated by BRENDA team
-
Go-alpha subunit
Manually annotated by BRENDA team
-
Jurkat leukemic T lymphocyte cell line, clone E6-1
Manually annotated by BRENDA team
-
cerebellar granule neuron
Manually annotated by BRENDA team
-
neonatal neuron
Manually annotated by BRENDA team
-
light-dependent localizations of the transducin-alpha subunit Gtalpha
Manually annotated by BRENDA team
-
light-dependent localizations of the transducin-alpha subunit Gtalpha
Manually annotated by BRENDA team
-
Go-alpha subunit
Manually annotated by BRENDA team
-
outer rod segment
Manually annotated by BRENDA team
-
outer rod segment
Manually annotated by BRENDA team
-
outer rod segment
Manually annotated by BRENDA team
-
rod outer segment
Manually annotated by BRENDA team
-
taste receptor cells
Manually annotated by BRENDA team
-
Go-alpha subunit
Manually annotated by BRENDA team
additional information
-
both Galpha12 and Galpha13 are expressed ubiquitously
Manually annotated by BRENDA team
additional information
-
expression patterns of GmGalpha1-4 are differentially regulated in different tissues of soybean and at various growth and development phases, e.g. during seed development and seed germination
Manually annotated by BRENDA team
additional information
-
expression of four Galpha, four Gbeta, and two Ggamma proteins, expression profiles by quantitative PCR during different developmental stages, overview. In general, the expression of G-protein genes is lower in roots than in aerial tissues. Except for GmGalpha4, which is highly expressed in the primary stem and the first trifoliate leaves at V1 stage, the soybean G-protein genes are expressed at comparable levels in all different developmental stages and tissue types
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
functional reconstitution of purified Gi and Go with m-opioid receptors in guinea pig striatal membranes
Manually annotated by BRENDA team
-
outer rod segment membrane
Manually annotated by BRENDA team
-
light-dependent localizations of the transducin-alpha subunit Gtalpha
Manually annotated by BRENDA team
-
light-dependent localization of transducin, colocalization of Gtalpha and LGN
Manually annotated by BRENDA team
-
light-dependent localizations of the transducin-alpha subunit Gtalpha
Manually annotated by BRENDA team
-
light-dependent localization of transducin, colocalization of Gtalpha and LGN
Manually annotated by BRENDA team
-
GmGalpha proteins
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
alpha,beta,gamma, 1 * 39000 + ? + ?, Go protein, SDS-PAGE; alpha,beta,gamma, 1 * 41000 + ? + ?, Gi protein, SDS-PAGE; alpha,beta,gamma, 1 * 45000-52000 + ? + ?, GS protein, SDS-PAGE
?
-
alpha,beta,gamma, 1 * 39000 + 1 * 36000 (beta1) + 1 * 80000 (gamma2), Go protein, SDS-PAGE; alpha,beta,gamma, 1 * 42000 + 1 * 36000 (beta1) + 1 * 8000 (gamma1), GL1 or Gq protein, SDS-PAGE; alpha,beta,gamma, 1 * 43000 + 1 * 36000, (beta1) + 1 * 8000 (gamma2), GL1 protein, SDS-PAGE
?
-
alpha,beta,gamma, 1 * 39000 + ? + ?, Go protein, SDS-PAGE; alpha, beta,gamma, 1 * 39000 + ? + ?, transducin, SDS-PAGE
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
-
heterotrimer
-
-
heterotrimer
-
existence of subunit-specific heterotrimers of G-proteins in soybean
additional information
-
G36 with a MW of 36000 Da determined by SDS-PAGE can be Gialpha or Goalpha. G50 with a MW of 50000 Da determined by SDS-PAGE can be Gsalpha
additional information
-
-
additional information
-
G proteins consist of three polypeptides: an alpha subunit that binds and hydrolyzes GTP, a beta subunit and a gamma subunit. The beta and gamma subunit form a dimer that only dissociates when it is denatured and is therefore a functional monomer. Structure of the subunits
additional information
-
interaction of enzyme with phospholipase Dalpha1, results stimulation of enzymic activity and inhibition of phopholipase activity
additional information
P63091
domain alpha2-4 and domain alpha3-beta5 are important for interaction with tubulin
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
lipoprotein
-
N-terminal palmitoylation and myristoylation of GmGa proteins
phosphoprotein
-
phosphorylation of Galpha subunits is an important modification that regulates their function. Galpha12 is a substrate for phosphorylation by protein kinase C. Endogenous Ga12 in human platelets is phosphorylated within the first 50 N-terminal amino acid residues in response to PMA, thrombin and the TXA2 receptor agonist U46619. Phosphorylated Galpha12 loses its affinity for Gbetagamma, and the association with Gbetagamma reciprocally inhibits the phosphorylation of Ga12 by protein kinase C. Endogenous Galpha13 in platelets is phosphorylated in response to PMA, although not in vitro. PKC-mediated phosphorylation of Ga13 in cell might require additional factors
side-chain modification
-
protein kinase K-like kinase phosphorylates G36 protein. The phosphorylation of G36 increases its Km for GTP by about 8fold without modification of Vmax. No significant modification after phosphorylation of G50 by protein kinase C or cAMP kinase
side-chain modification
-
betagamma subunit can be phosphorylated on His residues
lipoprotein
-
most Galpha subunits, excluding alphat, are S-palmitoylated at one or more Cys near the amino terminus, others, alphao, alphaz, alphai and alphat are N-myristoylated at Gly2 as well. Lipid modifications help bind alpha subunits to the plasma membrane, juxtaposing them to their cognate receptors and effector targets
lipoprotein
-
alpha subunits alphao, alphai and alphaz are myristoylated at the N-terminal Gly, alphas and alphaq are not myristoylated. Myristoylation is necessary for membrane attachment and facilitates binding of betagamma. It is an irreversible covalent modification and does not serve a regulatory role. Some alpha subunits are palmitoylated at Cys2. Palmitoylation is reversible. Activation of the beta-adrenergic receptor leads to rapid depalmitoylation of alphas, and depalmitoylated alphas does not activate adenylyl cyclase. Depalmitoylation might be a mechanism to turn off alphas and to sensitize the cell to beta-adrenergic stimulation
side-chain modification
-
subunits alphai-2 and alphaz can be phosphorylated on Ser or Thr in vivo and in vitro. Several types of subunits can be phosphorylated in vitro on Tyr residues by pp60c-src or by insulin receptor, changes in activity upon phosphorylation are modest at best
lipoprotein
-
both Galpha12 and 13 are subjected to palmitoylation at cysteine residues near their N-terminus, palmitoylation of Galpha13 is required for its association with the plasma membrane and its ability to activate RhoA through p115RhoGEF. Palmitoylated Galpha12 but not Galpha13 localizes in lipid rafts
additional information
-
Galpha12 and Galpha13 are not myristoylated because they lack a glycine residue as the second amino acid residue
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
P63091
crystal structure of mutant K180P-Galphai1 bound to a GTP analog
-
RGS4 complexed with Gialpha1-Mg2+-GDP-AlF4
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, Tris-HCl buffer, pH 7.8, 10 mM MgCl2, 50% v/v glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the alpha subunit of Gq family G proteins, GL1alpha(G14alpha), GL2alpha(G11alpha) and Gqalpha are expressed with G proteins beta1 and gamma2 subunits in insect cells using a baculovirus system. The trimeric forms of G proteins, GL1(GL1alphabetagamma), GL2(GL2alphabetagamma) and Gq(Gqalphabetagamma) are solubilized and purified
-
using Ni-NTA His-binding affinity chromatography and a Mono Q column
-
using a Ni-NTA column
-
purified from Sulfolobus solfataricus
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the alpha subunit of Gq family G proteins, GL1alpha(G14alpha), GL2alpha(G11alpha) and Gqalpha are expressed with G proteins beta1 and gamma2 subunits in insect cells using a baculovirus system. The trimeric forms of G proteins, GL1(GL1alphabetagamma), GL2(GL2alphabetagamma) and Gq(Gqalphabetagamma) are solubilized and purified
-
cloning of heterotrimeric G proteins, DNA and amino acid sequence determination and analysis
-
expression in Escherichia coli
-
Gtalpha and GtalphaR238E for expression in Escherichia coli strains DH5alpha and BL21(DE3)
-
into pcDNA3.1 vector for transfection of HEK-293 cells
-
into vector for expression in Escherichia coli
-
pBRH Gtalpha transgenic construct containing the mouse Gtalpha genomic sequence flanked by the mouse opsin promoter fragment and the polyadenylation signal, EE-tagged
-
Rab1a is cloned from a mouse cardiac cDNA library, adenoviruses expressing FLAG-Rab1a are generated for infection of rat ventricular myocytes
-
Expression of the N-terminally His6-tagged mutant Galphai/q chimeric gene, in which the native N-terminus of Galphaq is replaced with that of Galphai1, the gene also posseses a TEV cleavage site, amino acids 1-28 of rat Galphai1, a linker of Arg and Ser, and the 37-359 amino acid region of mouse Galphaq, expression of recombinant wild-type Galphaq and Galphaq mutant Q209E in Mus musculus Galphaq/11-deficient embryonic fibroblasts, Swiss3T3 cells, expression of alpha subunit cDNAs of heterotrimeric GTPases, Gs, Gi-2, G13 and G11 in human 293T cells
-
expressed in HEK-293T cells; Galpha subunit is subcloned into pcDNA3.1+
-
into the pT7-7 vector for expession in Escherichia coli JM109DE3 cells
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CFP-TM-Galpha
-
consists of a cleavable signal peptide from human growth hormone, enhanced CFP, the amino-terminal amino acids of the rat mu-opioid receptor, including TM1 and intracellular loop1, and the human Galpha subunit
CFP-TM-Galphai3
-
C to G mutation at the -4 position to render them insensitive to PTX-mediated ADP-ribosylation
CFP-TM-GalphaoA
-
C to G mutation at the -4 position to render them insensitive to PTX-mediated ADP-ribosylation
CFP-TM-GalphaQ205L
-
active mutant
CFP-TM-Galphasq5
-
the five aminoacids normally found in the carboxyl terminus of Galphas, QYELL, are replaced with those normally found in the carboxy terminus of Galphaq, EYNLV
R238E
-
mutant, reported to be a dominant-negative inhibitor of the rhodopsin-transducin-PDE visual system
S111N
-
mutation at carboxy-terminal end of helix alpha of helical domain, decreased nucleotide exchange kinetics, impaired adenylyl cyclase activation with GTPgammaS, but normal receptor and AlF4- activation
E92A, N93A, R519F
-
RGS14 mutant
E92A/N93A
-
RGS14 mutant
G202A
-
mutation of Galphai1 accelerates the rates of GTP hydrolysis and conformational change
G202A, K180P
-
mutations of Galphai1 accelerate the rates of GTP hydrolysis
GoLoco
-
RGS14 mutant
K180A
-
mutant of Galphai1, rate of GTP hydrolysis similar to wild-type
K180P
-
mutation of Galphai1 increases the rate of conformational change and decreases the rates of GTP hydrolysis
Myr-Pal-GoLoco
-
RGS14 mutant
Myr-Pal-GoLoco R519F
-
RGS14 mutant
R336L
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RGS14 mutant
R519F
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RGS14 mutant
RGS
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RGS14 mutant
RID-GoLoco
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RGS14 mutant
RID-GoLoco R336L
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RGS14 mutant
RID-GoLoco R519F
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RGS14 mutant
G208A
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mutant of G alphaQ, unable to release G betagamma-subunits
GtalphaQ200L
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GTPase-deficient mutant
I25A/E26A
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mutant of G alphaQ, lost ability to bind the G betagamma-subunits
Q209E
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increase of enzyme activity
Q209L
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increase of enzyme activity
R183C
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increase of enzyme activity
Rab1aN124I
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guanine nucleotide binding-deficient mutant
Q209E
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a Galphaq mutant, constructed for rasing of antibodies that specifically detect PMT-deaminated GTPase Galphaq
C351G
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mutation of Gi1alpha or Gi3alpha, pertussis toxin-resistant mutant
C352G
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mutation of Gi2alpha, pertussis toxin-resistant mutant
G223S
Saccharomyces pombe
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blocked interaction with regulator of G-protein signaling protein
Q244L
Saccharomyces pombe
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decreased GTPase activity
A26G
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mutant, rate of poly(U)-directed poly(Phe) synthesis and the ribosome-dependent GTPase activity are decreased, the catalytic efficiency of the intrinsic SsEF-2 GTPase triggered by ethylene glycol is enhanced
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
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mutants of transducin represent a major tool in designing potential therapeutical strategies for a group of visual diseases
medicine
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mutations in the gene for the alpha-subunit of cone transducin, GNAT2, cause cone-rod degeneration, CRD